ID   GPC5C_HUMAN             Reviewed;         441 AA.
AC   Q9NQ84; B5BUN4; Q2NL85; Q9NZG5;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 2.
DT   24-JAN-2024, entry version 173.
DE   RecName: Full=G-protein coupled receptor family C group 5 member C;
DE   AltName: Full=Retinoic acid-induced gene 3 protein;
DE            Short=RAIG-3;
DE   Flags: Precursor;
GN   Name=GPRC5C; Synonyms=RAIG3; ORFNames=PSEC0087;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, SUBCELLULAR
RP   LOCATION, AND INDUCTION.
RX   PubMed=10945465; DOI=10.1006/geno.2000.6226;
RA   Robbins M.J., Michalovich D., Hill J., Calver A.R., Medhurst A.D.,
RA   Gloger I., Sims M.A., Middlemiss D.N., Pangalos M.N.;
RT   "Molecular cloning and characterization of two novel retinoic acid-
RT   inducible orphan G-protein-coupled receptors (GPRC5B and GPRC5C).";
RL   Genomics 67:8-18(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR
RP   LOCATION, AND INDUCTION.
RX   PubMed=11311935; DOI=10.1016/s0167-4781(01)00197-x;
RA   Braeuner-Osborne H., Jensen A.A., Sheppard P.O., Brodin B.,
RA   Krogsgaard-Larsen P., O'Hara P.;
RT   "Cloning and characterization of a human orphan family C G-protein coupled
RT   receptor GPRC5D.";
RL   Biochim. Biophys. Acta 1518:237-248(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Placenta;
RX   PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA   Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA   Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA   Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA   Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA   Isogai T.;
RT   "Signal sequence and keyword trap in silico for selection of full-length
RT   human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT   libraries.";
RL   DNA Res. 12:117-126(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=19054851; DOI=10.1038/nmeth.1273;
RA   Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA   Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA   Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA   Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
RA   Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA   Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA   Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA   Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA   Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA   Nomura N.;
RT   "Human protein factory for converting the transcriptome into an in vitro-
RT   expressed proteome.";
RL   Nat. Methods 5:1011-1017(2008).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Ovary, and Pancreas;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA   Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA   Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344; SER-383 AND THR-423, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: This retinoic acid-inducible G-protein coupled receptor
CC       provide evidence for a possible interaction between retinoid and G-
CC       protein signaling pathways. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC       Cytoplasmic vesicle membrane; Multi-pass membrane protein.
CC       Note=Localized in the plasma membrane and perinuclear vesicles.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9NQ84-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NQ84-2; Sequence=VSP_037725;
CC   -!- TISSUE SPECIFICITY: Expression is highest in the periphery,
CC       particularly in the stomach, but also in the kidney, liver, pancreas,
CC       and prostate. In brain, levels of expression are generally lower than
CC       in the periphery, with the exception of cerebellum, spinal cord, and
CC       dorsal root ganglia (DRG). {ECO:0000269|PubMed:10945465,
CC       ECO:0000269|PubMed:11311935}.
CC   -!- INDUCTION: By all-trans retinoic acid (ATRA).
CC       {ECO:0000269|PubMed:10945465, ECO:0000269|PubMed:11311935}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH16860.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAI10849.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAI25081.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAI25082.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAG54752.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=CAC00633.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ276102; CAC00633.1; ALT_INIT; mRNA.
DR   EMBL; AF207989; AAF72870.1; -; mRNA.
DR   EMBL; BT007435; AAP36103.1; -; mRNA.
DR   EMBL; AK131210; BAG54752.1; ALT_INIT; mRNA.
DR   EMBL; AK075397; BAC11595.1; -; mRNA.
DR   EMBL; AB451470; BAG70284.1; -; mRNA.
DR   EMBL; AC079325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471099; EAW89163.1; -; Genomic_DNA.
DR   EMBL; BC016860; AAH16860.2; ALT_INIT; mRNA.
DR   EMBL; BC110848; AAI10849.1; ALT_INIT; mRNA.
DR   EMBL; BC125080; AAI25081.1; ALT_INIT; mRNA.
DR   EMBL; BC125081; AAI25082.1; ALT_INIT; mRNA.
DR   CCDS; CCDS11699.2; -. [Q9NQ84-1]
DR   RefSeq; NP_061123.3; NM_018653.3. [Q9NQ84-1]
DR   RefSeq; NP_071319.2; NM_022036.2. [Q9NQ84-1]
DR   AlphaFoldDB; Q9NQ84; -.
DR   BioGRID; 120980; 130.
DR   IntAct; Q9NQ84; 36.
DR   STRING; 9606.ENSP00000499092; -.
DR   ChEMBL; CHEMBL4523921; -.
DR   TCDB; 9.A.14.11.2; the g-protein-coupled receptor (gpcr) family.
DR   GlyCosmos; Q9NQ84; 1 site, No reported glycans.
DR   GlyGen; Q9NQ84; 1 site.
DR   iPTMnet; Q9NQ84; -.
DR   PhosphoSitePlus; Q9NQ84; -.
DR   SwissPalm; Q9NQ84; -.
DR   BioMuta; GPRC5C; -.
DR   DMDM; 46396014; -.
DR   EPD; Q9NQ84; -.
DR   jPOST; Q9NQ84; -.
DR   MassIVE; Q9NQ84; -.
DR   MaxQB; Q9NQ84; -.
DR   PaxDb; 9606-ENSP00000376403; -.
DR   PeptideAtlas; Q9NQ84; -.
DR   ProteomicsDB; 82101; -. [Q9NQ84-1]
DR   ProteomicsDB; 82102; -. [Q9NQ84-2]
DR   Antibodypedia; 31968; 251 antibodies from 29 providers.
DR   DNASU; 55890; -.
DR   Ensembl; ENST00000392627.7; ENSP00000376403.2; ENSG00000170412.18. [Q9NQ84-1]
DR   Ensembl; ENST00000392629.3; ENSP00000376405.3; ENSG00000170412.18. [Q9NQ84-1]
DR   Ensembl; ENST00000652294.1; ENSP00000498839.1; ENSG00000170412.18. [Q9NQ84-2]
DR   Ensembl; ENST00000709192.1; ENSP00000517544.1; ENSG00000291917.1. [Q9NQ84-1]
DR   Ensembl; ENST00000709195.1; ENSP00000517547.1; ENSG00000291917.1. [Q9NQ84-1]
DR   Ensembl; ENST00000709196.1; ENSP00000517548.1; ENSG00000291917.1. [Q9NQ84-2]
DR   GeneID; 55890; -.
DR   KEGG; hsa:55890; -.
DR   MANE-Select; ENST00000392627.7; ENSP00000376403.2; NM_022036.4; NP_071319.3.
DR   UCSC; uc002jkp.4; human. [Q9NQ84-1]
DR   AGR; HGNC:13309; -.
DR   CTD; 55890; -.
DR   DisGeNET; 55890; -.
DR   GeneCards; GPRC5C; -.
DR   HGNC; HGNC:13309; GPRC5C.
DR   HPA; ENSG00000170412; Tissue enhanced (liver, stomach).
DR   MIM; 605949; gene.
DR   neXtProt; NX_Q9NQ84; -.
DR   OpenTargets; ENSG00000170412; -.
DR   PharmGKB; PA28939; -.
DR   VEuPathDB; HostDB:ENSG00000170412; -.
DR   eggNOG; ENOG502QQEH; Eukaryota.
DR   GeneTree; ENSGT00950000182961; -.
DR   HOGENOM; CLU_044162_1_1_1; -.
DR   InParanoid; Q9NQ84; -.
DR   OMA; TIPQICC; -.
DR   OrthoDB; 4263681at2759; -.
DR   PhylomeDB; Q9NQ84; -.
DR   TreeFam; TF321410; -.
DR   PathwayCommons; Q9NQ84; -.
DR   SignaLink; Q9NQ84; -.
DR   BioGRID-ORCS; 55890; 8 hits in 1147 CRISPR screens.
DR   ChiTaRS; GPRC5C; human.
DR   GenomeRNAi; 55890; -.
DR   Pharos; Q9NQ84; Tbio.
DR   PRO; PR:Q9NQ84; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q9NQ84; Protein.
DR   Bgee; ENSG00000170412; Expressed in right lobe of liver and 147 other cell types or tissues.
DR   ExpressionAtlas; Q9NQ84; baseline and differential.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0043235; C:receptor complex; IDA:MGI.
DR   GO; GO:0031982; C:vesicle; HDA:UniProtKB.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; TAS:ProtInc.
DR   GO; GO:0030295; F:protein kinase activator activity; IBA:GO_Central.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR   CDD; cd15277; 7tmC_RAIG3_GPRC5C; 1.
DR   InterPro; IPR017978; GPCR_3_C.
DR   PANTHER; PTHR14511; G PROTEIN COUPLED RECEPTOR, CLASS C, GROUP 5; 1.
DR   PANTHER; PTHR14511:SF15; G-PROTEIN COUPLED RECEPTOR FAMILY C GROUP 5 MEMBER C; 1.
DR   Pfam; PF00003; 7tm_3; 1.
DR   PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
DR   Genevisible; Q9NQ84; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cytoplasmic vesicle;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW   Receptor; Reference proteome; Signal; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..441
FT                   /note="G-protein coupled receptor family C group 5 member
FT                   C"
FT                   /id="PRO_0000012967"
FT   TOPO_DOM        24..50
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        51..71
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        72..85
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        86..106
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        107..120
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        121..141
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        142..155
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        156..176
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        177..208
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        209..229
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        230..241
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        242..262
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        263..279
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        280..300
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        301..441
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          412..441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        412..430
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         344
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         383
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         403
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K3J9"
FT   MOD_RES         406
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K3J9"
FT   MOD_RES         414
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K3J9"
FT   MOD_RES         423
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1
FT                   /note="M -> MGTQPEPGLGARM (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10945465,
FT                   ECO:0000303|PubMed:19054851"
FT                   /id="VSP_037725"
FT   CONFLICT        204
FT                   /note="I -> V (in Ref. 1; CAC00633)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   441 AA;  48193 MW;  B255D9680328FE3D CRC64;
     MAIHKALVMC LGLPLFLFPG AWAQGHVPPG CSQGLNPLYY NLCDRSGAWG IVLEAVAGAG
     IVTTFVLTII LVASLPFVQD TKKRSLLGTQ VFFLLGTLGL FCLVFACVVK PDFSTCASRR
     FLFGVLFAIC FSCLAAHVFA LNFLARKNHG PRGWVIFTVA LLLTLVEVII NTEWLIITLV
     RGSGEGGPQG NSSAGWAVAS PCAIANMDFV MALIYVMLLL LGAFLGAWPA LCGRYKRWRK
     HGVFVLLTTA TSVAIWVVWI VMYTYGNKQH NSPTWDDPTL AIALAANAWA FVLFYVIPEV
     SQVTKSSPEQ SYQGDMYPTR GVGYETILKE QKGQSMFVEN KAFSMDEPVA AKRPVSPYSG
     YNGQLLTSVY QPTEMALMHK VPSEGAYDII LPRATANSQV MGSANSTLRA EDMYSAQSHQ
     AATPPKDGKN SQVFRNPYVW D
//